EP1920662A1 - Native potato protein isolates - Google Patents

Native potato protein isolates Download PDF

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Publication number
EP1920662A1
EP1920662A1 EP06077000A EP06077000A EP1920662A1 EP 1920662 A1 EP1920662 A1 EP 1920662A1 EP 06077000 A EP06077000 A EP 06077000A EP 06077000 A EP06077000 A EP 06077000A EP 1920662 A1 EP1920662 A1 EP 1920662A1
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EP
European Patent Office
Prior art keywords
isolate
potato protein
protein
patatin
native potato
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Withdrawn
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EP06077000A
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German (de)
English (en)
French (fr)
Inventor
Marco Luigi Frederico Giuseppin
Catrinus Van Der Sluis
Marc Christiaan Laus
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Cooperative Avebe UA
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Cooperative Avebe UA
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Priority to EP06077000A priority Critical patent/EP1920662A1/en
Priority to PT07103954T priority patent/PT1974615E/pt
Priority to AT07103954T priority patent/ATE451842T1/de
Priority to DE602007003805T priority patent/DE602007003805D1/de
Priority to DK07103954.9T priority patent/DK1974615T3/da
Priority to PL07103954T priority patent/PL1974615T3/pl
Priority to EP07103954A priority patent/EP1974615B1/en
Priority to CA2669096A priority patent/CA2669096C/en
Priority to US12/513,971 priority patent/US8465911B2/en
Priority to DK07870596.9T priority patent/DK2083635T3/da
Priority to US12/514,322 priority patent/US9526266B2/en
Priority to CA2669152A priority patent/CA2669152C/en
Priority to EP07834645.9A priority patent/EP2083636B1/en
Priority to US12/514,249 priority patent/US8486481B2/en
Priority to PCT/NL2007/050512 priority patent/WO2008069649A1/en
Priority to PL07870595T priority patent/PL2083634T3/pl
Priority to DK07870595.1T priority patent/DK2083634T3/en
Priority to PCT/NL2007/050515 priority patent/WO2008069651A1/en
Priority to DK07834645.9T priority patent/DK2083636T3/da
Priority to PCT/NL2007/050514 priority patent/WO2008056977A1/en
Priority to PCT/NL2007/050513 priority patent/WO2008069650A1/en
Priority to CA2669212A priority patent/CA2669212C/en
Priority to EP07870596.9A priority patent/EP2083635B1/en
Priority to PL07870596T priority patent/PL2083635T3/pl
Priority to PL07834645T priority patent/PL2083636T3/pl
Priority to EP07870595.1A priority patent/EP2083634B1/en
Priority to CA2669090A priority patent/CA2669090C/en
Priority to US12/514,210 priority patent/US9102749B2/en
Publication of EP1920662A1 publication Critical patent/EP1920662A1/en
Priority to US13/919,802 priority patent/US20130281669A1/en
Priority to US14/722,906 priority patent/US9968118B2/en
Withdrawn legal-status Critical Current

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    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L29/00—Foods or foodstuffs containing additives; Preparation or treatment thereof
    • A23L29/20—Foods or foodstuffs containing additives; Preparation or treatment thereof containing gelling or thickening agents
    • A23L29/206—Foods or foodstuffs containing additives; Preparation or treatment thereof containing gelling or thickening agents of vegetable origin
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
    • A23J1/006—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from vegetable materials
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
    • A23J1/16—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from waste water of starch-manufacturing plant or like wastes
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J3/00—Working-up of proteins for foodstuffs
    • A23J3/14—Vegetable proteins
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L2/00—Non-alcoholic beverages; Dry compositions or concentrates therefor; Their preparation
    • A23L2/52—Adding ingredients
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L2/00—Non-alcoholic beverages; Dry compositions or concentrates therefor; Their preparation
    • A23L2/52—Adding ingredients
    • A23L2/66—Proteins
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
    • A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
    • A23L33/17—Amino acids, peptides or proteins
    • A23L33/185—Vegetable proteins
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
    • A61K47/30—Macromolecular organic or inorganic compounds, e.g. inorganic polyphosphates
    • A61K47/42—Proteins; Polypeptides; Degradation products thereof; Derivatives thereof, e.g. albumin, gelatin or zein
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/415—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from plants
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
    • A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs

Definitions

  • the invention relates to a process for native potato protein isolation, to native potato protein isolates, to the use thereof, and to a food, nutraceutical and pharmaceutical product comprising a native potato protein isolate.
  • potato fruit juice The undiluted juice from potato tuber is called potato fruit juice.
  • Potato fruit juice may be produced by washing and rasping potatoes and separating the starch and fibres by various techniques, such as centrisieves, hydrocyclones and decanters.
  • Fresh potato fruit juice is a complex mixture of soluble and insoluble material comprising proteins, starch, minerals, toxic glycoalkaloids and monomeric and polymeric reactive phenols.
  • Fresh potato fruit juice is however not very stable. Oxidation leads to conversion of phenolic compounds into quinones which rapidly combine into a dark polymer residue. During the oxidation process reaction the potato proteins can partially cross-link, which dramatically reduces the solubility of the proteins. The complexity and instability of the potato fruit juice makes the separation and isolation of minimally denatured or modified proteins a complicated and economically demanding process.
  • Native potato proteins can tentatively be divided into three classes (i) the patatin family, highly homologous acidic 43 kDa glycoproteins (40-50 wt.% of the potato proteins), (ii) basic 5-25 kDa protease inhibitors (30-40 wt.% of the potato proteins) and (iii) other proteins mostly high molecular weight proteins (10-20 wt.% of the potato proteins) ( Pots et al., J. Sci. Food. Agric. 1999, 79, 1557-1564 ). Potato protein is rich in lysine and may form an excellent supplement for lysine-poor proteins such as those of cereal. The nutritional value of total potato protein have been shown to be greater than that of casein and comparable to that of whole egg white protein.
  • Patatin is a family of glycoproteins that have lipid acyl hydrolase and transferase activities and accounts for up to 40 wt.% of the total soluble protein in potato tubers.
  • protease inhibitors can be divided into different groups based on their molecular weight.
  • the different groups of protease inhibitors are identified as protease inhibitor I (molecular weight of about 39 kDa), carboxypeptidase inhibitor (molecular weight of about 4 100 Da), protease inhibitors IIa and IIb (molecular weight of about 20.7 kDa), and protease inhibitor A5 (molecular weight of about 26 kDa).
  • the ratio of these different groups of protease inhibitors in the total potato protein depends on the potato variety. Protease inhibitors from potato have a broad range of potentially important applications.
  • Protease inhibitors have for instance shown to be useful in the treatment of diabetes, for eliciting satiety in mammals, for reducing the risk of skin cancer, for inhibiting the growth of bacteria, and for preventing or treating inflammation on pruritis of skin and intestine, see for instance WO-A-99/059623 .
  • potato protein is currently only used as animal feed, because the available products exhibit a number of serious drawbacks.
  • native potato protein is used in this application is meant to refer to the potato protein without any significant physical or (bio)chemical modification or inactivation, in particular denaturation.
  • Existing methods for isolating potato proteins and potato protein fractions include fractionation, ion exchange, gel permeation, ultrafiltration, affinity and mixed-mode chromatography and fractionation by heat coagulation.
  • a disadvantage of these prior art isolation methods is that they lack a strict pH control to maintain good potato protein characteristics. Furthermore, they do not sufficiently deal with undesirable contaminants. In particular, glycoalkaloid contaminants are not sufficiently removed.
  • Glycoalkaloids are well-known anti-nutritional factors.
  • the glycosylated forms (such as ⁇ -solanine and ⁇ -chaconine) show the highest toxicity.
  • the aglycons (such as solanidine), have a more than 100 fold lower liver toxicity.
  • Solanine and derivatives constitute for more than 95 % of the glycoalkaloids in the potato.
  • Other glycoalkaloids include for example tomatine, tomatidenol and demissidine.
  • Glycoalkaloids have a bitter taste and negatively affect many of the physical and/or biological properties of the proteins, especially when the pH is increased by adhering to the soluble proteins as shown in this application.
  • the taste threshold is about 140-170 mg of glycoalkaloids expressed as ⁇ -solanine per kg product. This threshold strongly limits the applications of prior art native potato protein isolates in foods.
  • glycoalkaloids such as ⁇ -solanine at pH values typically above 6.2 results in an excessive adherence of glycoalkaloids and other compounds, such as polyphenols, to the potato proteins.
  • Partial removal of glycoalkaloids has been achieved by various ultrafiltration methods at excessive diafiltration conditions, see for instance WO-A-97/42834 .
  • the HPLC method employed Houben et al., J. Chromatogr. A 1994, 661, 169-174 ) does not detect the aglycons that are formed by enzymatic hydrolysis after prolonged processing of potato fruit juice as described.
  • Ultrafiltration can remove some glycoalkaloids and salts, but does not remove high molecular contaminants, such as polyphenols and proanthocyanidines and coloured derivatives thereof, such as epicatechins and anthocyanines, that are formed at pH values below 4.5.
  • Glycoalkaloids can also be removed by enzymatic hydrolysis. However, this does not lead to removal of aglycon, which also binds to the potato proteins with negative effects on their physical and/or biological properties. Therore, both a HPLC method ( Kodamatani et al., J. Chromatogr. A 2005, 110, 26-31 ) and a colorimetric method ( Walls et al., J. Chem. Ecol. 2005, 31, 2263-2288 ) must be used to measure the main glycoalkaloids, the total glycoalkaloids and the aglycons, respectively.
  • Glycoalkaloid removal by fermentation is not considered relevant for safe native protein production. Conversion by fermentation causes severe technical issues to implement this process at a commercial scale. The bioconversions are costly and have a low productivity. The micro-organisms employed and hygiene form a limitation for the application of the derived products for foods.
  • Pectins typically lead to flocculation of the isolate at pH values below 5.0.
  • Contaminants, such as polyphenols, in the patatin fraction lead to very variable physical properties in terms of colour and solubility at various pH.
  • the presence of protease inhibitor and other contaminants with a surface active function in the patatin fraction has a negative effect on the good emulsifying and gelling properties of patatin.
  • further purification of the patatin fraction improves the foaming and emulsification properties, as well as the foaming and emulsion stability of patatin.
  • a protease inhibitor fraction containing patatin contaminants is less useful in e.g. pharmaceutical applications.
  • Object of the invention is to provide a process that allows for an excellent isolation of native total potato protein and native potato protein patatin and protease inhibitor fractions in pure form.
  • a further object of the invention is to provide native potato protein isolates that have a high solubility at various pH values and are essentially free from undesired contaminants.
  • the invention provides an isolation process for native potato proteins. Accordingly, the invention is directed to a process for obtaining a native potato protein isolate comprising patatin and protease inhibitor, comprising the steps of
  • the process according to the invention leads to a highly pure native potato protein isolate with a minimum of denatured protein and stable solubility.
  • the potato fruit juice is pre-treated with a divalent metal cation at a pH of 7-9, preferably 7.0-7.5, to flocculate undesired material, followed by a separation of the flocks by centrifugation.
  • a particularly suitable divalent metal cation is Ca 2+ . It has been found that this pre-treatment removes undesired material such as negatively charged polymers, pectins, glycoalkaloids, and micro-organisms from the potato fruit juice. In particular, the removal of pectins and glycoalkaloids is advantageous, since these compounds adhere to the potato proteins and may cause flocculation. These compounds thus lead to an unstable protein isolate.
  • the supernatant is subjected to expanded bed adsorption chromatography.
  • This technique is described in WO-A-2004/082397 , which document is hereby incorporated by reference.
  • a moderately high flow rate typically in the range of 600-1 200 cm/h.
  • the expanded bed adsorption chromatography is operated at a pH of less than 11, preferably at a pH of less than 10.
  • the native potato proteins in the pre-treated potato fruit juice are isolated from the supernatant by binding them onto a suitable adsorbent in the expanded bed adsorption column.
  • Column materials that bind native potato proteins include mixed-mode adsorbentia such as Amersham StreamlineTM Direct CST I (GE Healthcare), Fastline adsorbentia (Upfront Chromatography A/S), macroporous adsorbentia such as AmberliteTM XAD7HP (Röhm & Haas Company) and ion exchange adsorbents (for patatin isolates and purification see G. Koningsveld, "Physico-chemical and functional properties of potato proteins", PhD thesis, Wageningen University, Wageningen, The Netherlands, 2001 ; for protease inhibitor isolates see L.
  • mixed-mode adsorbentia such as Amersham StreamlineTM Direct CST I (GE Healthcare), Fastline adsorbentia (Upfront Chromatography A/S), macroporous adsorbentia such as AmberliteTM XAD7HP (Röhm & Haas Company) and ion exchange adsorbents (for
  • the adsorbent with adsorbed native potato proteins is subsequently eluted with a suitable eluent in order to retrieve the native potato protein isolate.
  • the eluent preferably has a pH in the range of 4-12, more preferably in the range of 5.5-9.0.
  • the native potato protein isolate has an isoelectric point above 4.8, a molecular weight of more than 5 kDa and a glycoalkaloid concentration of less than 150 ppm.
  • the proteins can be fractionated to both isoelectric point and molecular weight. This allows to separate the patatin and protease inhibitor fractions.
  • Patatin isolates are eluted at a pH of 5.7-8.7, preferably at a pH of 5.8-6.2.
  • Protease inhibitors are eluted at a pH of 5.8-12.0, preferably at a pH of 6.0-9.5.
  • the mixed-mode adsorbentia can be used in two modes.
  • the first mode is selective elution, which comes down to binding of essentially all of the potato protein and subsequently eluting a first desired potato protein fraction with an appropriate buffer and eluting a second desired potato protein fraction with another appropriate buffer.
  • the second mode is selective adsorption, which comes down to binding of a first desired potato protein fraction on one column at an elevated pH, and adjusting the effluent to a lower pH so that a second desired potato protein fraction can bind on a second column.
  • Selective elution is described in the examples. Selective adsorption for instance involves passing a potato fruit juice at pH 5.0-7.0, typically at pH 6.0, over a first column to bind the protease inhibitor fraction.
  • the protease inhibitor fraction may be eluted using an appropriate buffer as described above.
  • the effluent of the first column is adjusted to a pH of 4.5-5.0, preferably to a pH of 4.8, and passed over a second column to bind the patatin fraction. Patatin is eluted using an appropriate buffer as described above. Selective adsorption yields a robust processing and higher purity of the isolates than selective elution.
  • the native potato proteins may advantageously be concentrated by ultrafiltration. This may further reduce the amount of remaining glycoalkaloids.
  • the choice of the ultrafiltration membrane material can strongly influence the selectivity.
  • the ultrafiltration membrane is negatively charged and comprises regenerated cellulose, polyethersulphones and polysulphones (PES).
  • Protease inhibitors isolates may be concentrated using PES based membranes with a molecular cut-off of 2-20 kDa, and to some extent 30 kDa.
  • Patatin isolates may be concentrated using PES based membranes with a molecular cut-off of 5-30 kDa or a regenerated cellulose based membrane with a molecular cut-off of 5-30 kDa.
  • These membranes can be implemented as tubular, spiral wound, hollow fibre, plate and frame, or as cross-rotational induced shear filter units.
  • Ultrafiltration membranes should be operated at conditions to both concentrate and remove glycoalkaloids effectively.
  • the pH values should be below pH 6.2.
  • glycoalkaloids such as ⁇ -solanine
  • Patatin isolates are ultrafiltrated at pH values of 4.0-6.0, preferably pH 4.5-5.4.
  • pH values of 3-7 preferably 3.2-4.5 are used. After removal of glycoalkaloids the pH can be increased to pH 7-10 to enable high fluxes through the membranes.
  • Protease inhibitors are preferably processed at low pH of 3.0-5.0.
  • the native potato protein isolate thus obtained is essentially free from toxic components and colour.
  • the isolate is further organoleptically neutral and stable.
  • An ion-exchange step may be applied to isolate protease inhibitors or patatin with an alkaline or acid elution. Residual glycoalkaloids and taste and colour may be removed using ion-exchange, polymer adsorbents (such as AmberliteTM and Polyclar ® ) and mineral adsorbents (such as zeolites, activated carbon and bleach earth).
  • polymer adsorbents such as AmberliteTM and Polyclar ®
  • mineral adsorbents such as zeolites, activated carbon and bleach earth.
  • the native potato protein isolates obtained by the process of the invention may be concentrated up to more than 20 % dry matter by evaporation, freeze concentration, or isoelectric precipitation using carbondioxide.
  • the dry matter of these concentrates can contain more than 85 % of protein, preferably more than 90 % of protein, based on the nitrogen level (Kjeldahl nitrogen content times 6.25).
  • the dried products can contain more than 90 %, preferably more than 92 % of protein, with a moisture level of 4-9 %.
  • the invention is further directed to a process in which a native potato protein protease inhibitor isolate is processed into at least one isolate selected from the group consisting of a protease inhibitor I isolate, a carboxypeptidase inhibitor isolate, a protease inhibitor IIa and IIb isolate, and a protease inhibitor A5 isolate.
  • This processing can involve ion exchange or gel permeation chromatography.
  • the patatin isolate is a preferred source of various valuable enzymes, such as alkaline phosphorylase ( US-A-0 290 952 ), apyrase, lipoxygenase, and polyphenol oxidase. Therefore, the patatin isolate has a wide range of applications in food, fine chemical and pharmaceutical industry.
  • the invention is directed at the native potato protein isolate obtainable by the process according to the invention.
  • This native potato protein isolate includes the total native potato protein isolate, the native potato protein patatin isolate, and the native potato protein protease inhibitor isolate. These potato protein isolates are characterised by their high degree of purity and stability.
  • the total native potato protein isolate of the invention can have an isoelectric point above 4.8, a molecular weight of more than 5 kDa, and a glycoalkaloid concentration of less than 150 ppm.
  • the isolate is preferably essentially free of organic acids and amino acids.
  • the native potato protein patatin isolate of the invention can have an isoelectric point of below 5.8, preferably 4.8-5.5, a molecular weight of more than 30 kDa, preferably more than 35 kDa, and a glycoalkaloid concentration of less than 150 ppm.
  • the native potato protein protease inhibitor isolate of the invention can have an isoelectric point above 5.5, preferably above 5.8, a molecular weight of below 35 kDa, preferably 5-30 kDa, and a glycoalkaloid concentration of less than 150 ppm.
  • Dry native potato proteins can be obtained by spray drying, flash drying or freeze drying.
  • the patatin isolate and total protein isolate are set at a suitable pH to ensure good water solubility.
  • the pH of the concentrates is set to 7.0-9.0, preferably to 7.0-8.0.
  • Concentrates of protease inhibitors can be spray dried using both low pH (3.0-4.0) as well as high pH values (7.0-9.0).
  • the native potato proteins thus obtained have a water solubility of more than 90 %, preferably more than 95 % at a pH of 7.0 and a temperature of 25 °C. Solubility is expressed as the percentage of protein in the supernatant after centrifugation of the solution.
  • the native potato protein isolate as obtained after ultrafiltration concentration has a protein content of more than 75 % of the dry matter content.
  • the protein content herein is defined as Kjeldahl nitrogen content times 6.25.
  • the protein content in the native potato protein isolate is more than 80 %, more preferably more than 90 %, and even more preferably more than 95 %.
  • the inventors further found that the invention allows to obtain a native potato protein isolate with a low sulphite content of less than 10 ppm.
  • Such native potato protein isolate can be safely used in foods, in contrast to the potato protein isolate of WO-A-97/42834 to which large amounts of sulphite are added during ultrafiltration.
  • the native potato protein isolates of the invention may be characterised by a two-dimensional gel electrophoresis analysis combined with an identification of the key proteins in the isolate using MALDI-TOF mass spectrometry analysis.
  • the proteins can be separated in the two-dimensional gel electrophoresis using a pH gradient from 3 to 8 and a molecular weight of 5-100 kDa.
  • the invention is directed to the use of a native potato protein patatin isolate as a gelling agent, an emulsifier or foaming agent in a food product. It was found that the gelling, emulsifying and foaming properties of the patatin fraction of the native potato protein isolate according to the invention are enhanced due to the high purity of the isolate.
  • the invention also relates to the use of a native potato protein patatin isolate as a source of pharmaceutical and therapeutic enzymes.
  • the invention is further directed to a food product comprising a native potato protein isolate according to the invention.
  • Typical food products include for instance dairy products, ice cream, bakery products, meringues.
  • the nutritional value of the potato proteins is very high and comparable to hen egg protein. This is based on amino acid composition and the experience of these proteins as feed proteins. Its high nutritional value combined with the absence of antinutritional glycoalkaloid compounds makes the native potato protein product a very suitable ingredient for infant foods, sports drinks and derived protein hydrolysates.
  • the invention is also directed to a personal care product comprising a native potato protein isolate according to the invention, such as a skin care cream.
  • native potato protein isolates of the invention may be advantageously used in the following applications.
  • the foam stability is calculate by measuring the volume after 15 and 30 minutes according to the following formula.
  • the sample is dissolved at the desired pH and an emulsion is prepared with a blender (Ultra Turrax) at 10 000 rpm.
  • a blender Ultra Turrax
  • the gel strength is determined using a Texture Analyser (TA-HDi Texture Analyser, Stable Micro Systems) with a P75 probe in 40 ml vials.
  • TA-HDi Texture Analyser Stable Micro Systems
  • the protein samples are dissolved for 2 hours with a magnetic stirrer in a 40 ml sample flask at 20 °C.
  • the parameters of the texture analyser were set as follows: pre-test speed: 1.00 mm/s, test speed: 0.10 mm/s, post test speed: 2.00 mm/s, distance: 25.0 mm, load cell: 5 kg.
  • Method 8 Total protein content purification using ultrafiltration.
  • Example 1 Comparison of the basic properties of native potato protein isolates using various methods Method 1 2 3 4 5 6 7 8 9 10 11 Amersham patatin 1 Amersham PI 2 Amersham total 3 Amberlite total 4 Heat coag. total 5 Acid coag. patatin 6 Acid coag.
  • N.A. means not applicable.
  • Solubility is defined as the amount of dry weight protein that can be suspended in water. This is expressed as % of protein in the supernatant after centrifugation of the solution. Solubility is measured for a 3 % (w/v) protein solution. "+” means good solubility (> 85 %); “+/-” means moderate solubility (a suspension is formed with a solubility of between 60 and 85 %); - means low solubility (between 25 and 60 %); "--" poor solubility less than 25 % dissolves and precipitates). The solubility strongly depends on the type of drying method and the pH of the protein concentrate prior to drying.
  • Solubility stability Stability of the soluble protein solution is defined as the condition of being stable or resistant to changes for at least 7 days at room temperature.
  • Microbial stable solutions are obtained by removing contaminating micro-organisms by microfiltrating the samples through a 0.22 ⁇ m. After solubilising the protein it either precipitates, dissolves or forms a suspension.
  • the stability describes the state of the solution over at least 7 days since solubilising. For example, at day 1 some dry product dissolves and forms a clear solution. If it is still a clear solution after 7 days it is marked "+" for stability. If there is a lot of precipitation visible after 7 days, it gets a "-". Intermediate states would get a "+/-".
  • Solubility (as defined in a) for a protein solution of 3 % at pH values between 5 and 7.
  • d Colour of the solution Visual appearance of a 3 % protein solution at pH 7.0.
  • e Colour stability Stability (as defined in b) of the colour of the protein solution for at least 7 days. If the colour does not change during 7 days, it gets a "+”. If it changes dramatically, a "-" is used. Minor colour changes get a "+/-”.
  • "++” means excellent stability; "+” means good stability; “+/-” means moderate stability; "-” means low stability f Odour of the protein solution The odour is determined by a trained panel.
  • i Glycoalkaloid content Total amount of glycoalkaloids in the protein solution is measured by the method described by Walls et al. (2005). "++” means very low TGA ( ⁇ 150 ppm); “+” means low TGA (between 150-400 ppm); “+/-” means intermediate TGA (between 400-1 000 ppm) ; “-” means high TGA (> 1 000 ppm).
  • the HPLC method of Kodamatani et al. is used for specific glycoalkaloids.
  • Polyphenols are determined using the Folin-Denis method (Official methods of analysis of the AOAC 7 th edition 1950).
  • Figure 1A shows an SDS-PAGE comparison of the following potato protein isolates.
  • Patatin migrates at a molecular weight of 40-41 kDa.
  • Protease inhibitors migrate at molecular weights of 5-22 kDa.
  • Line 3 shows partial degradation products of patatin.
  • the gel strength N was determined of patatin and protease inhibitor isolate gels that were prepared with different protein content, different pH values and different ionic strengths. The results are shown in the following table. Protein content (%) pH Ionic strength (mM) Patatin isolate gel strength Protease inhibitor gel strength 5.00 5.0 125 0.154 0.025 7.50 5.0 125 5.600 0.020 10.00 5.0 125 1.597 0.237 7.5 3.0 125 0.196 0.101 7.5 7.0 125 1.554 0.161 7.5 5.0 50 0.970 0.166 7.5 5.0 200 0.783 0.096
  • patatin isolates gel better and have superior gelling properties in a pH range of 4.8 - 5.5.
  • the patatin isolate gives a very pronounced strong gel at pH 5.0 near the iso-electric point of the patatins in that isolate. This makes it very suitable for slightly acidified food products such as yoghurts.
  • the emulsion activity EA and the emulsion stability ES were determined of protease inhibitor and patatin isolate emulsions that were prepared with different protein content, different oil content, different pH values and different ionic strengths.
  • the native potato protein isolates were obtained according to method 11. The results are shown in the following table.
  • patatin isolates give a good emulsion and emulsion stability depending on the ionic strenght pH and protein content used. The differences between the protease inhibitor isolates and patatin isolates are small.
  • the relative gel strength was determined in 20 mM sodium phosphate buffer at pH 7.0. The relative strength was scaled between 0 to 14. A value of 14 corresponds with a gel of 20 % egg white protein.
  • the following high grade proteins were used:
  • Patatin fraction yields a transparent gel at a unique low concentration of 5-8 %. Milk proteins and egg white proteins form gels at concentrations above 8 %.
  • the solubility of patatin isolate till turbidity occurs at pH 7.0 is 5 %.
  • Patatin isolate has a relatively low gelling concentration threshold of 5 % at pH 7.0. Patatin isolates form opaque gels at a pH equal or lower than 7.0 and at an ionic strength of more than 25 mM.
  • FIG. 4 shows the effect of the pH on the gel transparency.
  • a clear gel is formed between a pH of 7.0 and 8.0 and at a patatin fraction concentration of 5-8 %.
  • the concentration at which clear gels are formed can be controlled by adding small amounts of charged surfactants in a molar ratio of 0.8-3.0.
  • a 1 to 1 molar ratio of patatin fraction : sodium dodecyl sulphate gives a clear gel at 10 % vs. an opaque gel at 10 % without sodium dodecyl sulphate.
  • Example 6 The application of the potato isolates in light bakery products such as meringues
  • Meringues consist of sugar and protein isolates and are representative of bakery foam products. Isolates of patatin, protease inhibitor and total protein were compared with egg albumin. The potato protein isolates were prepared using isolation method 9, 10 and 11. The chromatography was performed at semi-tech 35 liter scale. All samples were white powders with good solubility and contained more than 90 % of protein based in nitrogen content times 6.25 and a glycoalkaloid level of less than 150 ppm. The mixture mentioned in the recipe was stirred with a Hobart mixer. The overrun was determined as the volume of the total mixture foam before and after stirring. The viscosity was determined with a Brookfield viscometer with a spindle S 93. The texture was analysed with a Stevens LFRA texture analyser.
  • meringues For the preparation of the meringues, 150 g of egg albumin protein, or a solution of 10 % potato protein isolate and 90 % water, and 75 g of sugar were whipped up and baked as follows.
  • Patatin, protease inhibitor and total protein isolates give a better overrun than egg albumin.
  • the texture and the viscosity is slightly lower than egg albumin.
  • the patatin isolate is comparable with the egg albumin. This means that the patatin is very suitable for foaming applications. The high overrun values show that the patatin isolate is significant more effective than egg albumin.
  • Protease inhibitor and total protein isolates are less suitable for applications with sugar-rich foam, because they are less stabile with a lower viscosity.
  • the meringues prepared with protease inhibitor isolate show a very soft and brittle final product. The baked product becomes soft within one hour after baking. The protease inhibitor fraction is therefore not suitable for these types of foamy products. The shorter whipping time however gives advantages in some applications where foams are used quickly with low amounts of shear. Blending of protease inhibitor fraction with other structuring proteins may be considered.
  • Total protein isolate gives a lower performance due to the effects of the protease inhibitor in the isolate. All potato protein isolates show a very bland flavour after baking. Especially patatin results in a crispy meringues structure. Patatin isolate produces a very good foam and meringues and is a very effective substitute for egg albumin. It has distinct and superior properties compared with total potato protein isolates and protease inhibitor isolates.
  • the patatin isolate showed a high protein content of 95 %. This is higher than the high grade whey and egg white proteins that show a protein content in the range of 81 to at most 92 %.
  • the solubility of an adequately dried patatin isolate of 92 % is comparable to high grade whey and egg white proteins that show a solubility of 97-100 %.
  • Example 8 Foaming capacity of potato protein isolates at several pH values in water with low ionic strength
  • Potato protein isolates as described in method 9, 10 and 11 were used. A protein solution is shaken to form a foam layer. The amount of formed foam depends on the protein concentration and on the pH of the solution. 100 ml of protein solution at several concentrations in the range of 0.1 % - 5.0 % (w/v), at pH 3.0, 5.0 and 7.0, were added to a Stedum flask and vigorously shaken for 30 seconds. The foam capacity for each protein was plotted as a function of the protein concentration (in g/l). The results as shown in Figures 5-10. The results for patatin are shown in Figures 5 and 6. Figure 5 shows that the largest amounts of foam are formed at a pH of 3.0. This is especially the case at patatin concentrations below 1 g/l.
  • patatin has its best foaming capacity at a pH of 3.0. No significant differences in foaming properties were observed between pH 5.0 and 7.0. The results for protease inhibitor are displayed in Figures 7 and 8. It seems that the pH did not have any influence on the foam capacity. In contrast to patatin, no decrease of foam formation is observed at higher protein concentrations. In fact, at 5 g/l the formed foam is ten times higher than for patatin. This would indicate that the foaming capacity for protease inhibitors would be ten times higher than for patatin.
  • the results for total protein isolate are shown in Figures 9 and 10.
  • the protease inhibitor isolates show the highest foaming capacity compared to patatin isolates and total protein isolates.
  • the foaming capacity is not very sensitive to pH. Only the total protein isolate shows a significant pH dependency with an optimum at pH 3.0.
  • Example 9 Basic appearance of protease inhibitor isolate gels as a function of pH and ionic strength
  • protease inhibitor isolate the protein solution has variable appearance in its gelling properties depending on the pH and the ionic strength.
  • the appearance after a treatment for 1 hour at a temperature of 80 °C is shown in Figure 11.
  • the diagram summarises the appearance for a 4-8 % protease inhibitor solution.
  • Protease inhibitor isolate yields a transparent gel at a unique low concentration of 4 % and a pH.
  • the solubility of protease inhibitor isolate till turbidity occurs at pH 3.5 is > 25 %.
  • Protease inhibitor isolate has a relatively low gelling concentration threshold of 4 % at pH 3-4.4
  • Protease inhibitor isolates form opaque gels at a pH equal or lower than 4.3 and at an ionic strength of more than 125 mM. Above pH 4.5 protease inhibitor isolates yield stable milky solutions.

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EP06077000A EP1920662A1 (en) 2006-11-10 2006-11-10 Native potato protein isolates
PT07103954T PT1974615E (pt) 2006-11-10 2007-03-12 Formação de um gel à base de proteína
AT07103954T ATE451842T1 (de) 2006-11-10 2007-03-12 Proteingelbildung
DE602007003805T DE602007003805D1 (de) 2006-11-10 2007-03-12 Proteingelbildung
DK07103954.9T DK1974615T3 (da) 2006-11-10 2007-03-12 Proteingeldannelse
PL07103954T PL1974615T3 (pl) 2006-11-10 2007-03-12 Wytwarzanie żelu białkowego
EP07103954A EP1974615B1 (en) 2006-11-10 2007-03-12 Protein gel formation
PL07870595T PL2083634T3 (pl) 2006-11-10 2007-10-25 Izolaty natywnego białka ziemniaka
PCT/NL2007/050513 WO2008069650A1 (en) 2006-11-10 2007-10-25 Native potato protein isolates
DK07870596.9T DK2083635T3 (da) 2006-11-10 2007-10-25 Glycoalkaloid fjernelse
US12/514,322 US9526266B2 (en) 2006-11-10 2007-10-25 Glycoalkaloid removal
CA2669152A CA2669152C (en) 2006-11-10 2007-10-25 Glycoalkaloid removal
EP07834645.9A EP2083636B1 (en) 2006-11-10 2007-10-25 Glycoalkaloid removal
US12/514,249 US8486481B2 (en) 2006-11-10 2007-10-25 Glycoalkaloid removal
PCT/NL2007/050512 WO2008069649A1 (en) 2006-11-10 2007-10-25 Protein gel formation
CA2669096A CA2669096C (en) 2006-11-10 2007-10-25 Native potato protein isolates
DK07870595.1T DK2083634T3 (en) 2006-11-10 2007-10-25 NATIVE POTATO PROTEIN ISOLATES
PCT/NL2007/050515 WO2008069651A1 (en) 2006-11-10 2007-10-25 Glycoalkaloid removal
DK07834645.9T DK2083636T3 (da) 2006-11-10 2007-10-25 Glycoalkaloid fjernelse
PCT/NL2007/050514 WO2008056977A1 (en) 2006-11-10 2007-10-25 Glycoalkaloid removal
US12/513,971 US8465911B2 (en) 2006-11-10 2007-10-25 Native potato protein isolates
CA2669212A CA2669212C (en) 2006-11-10 2007-10-25 Glycoalkaloid removal
EP07870596.9A EP2083635B1 (en) 2006-11-10 2007-10-25 Glycoalkaloid removal
PL07870596T PL2083635T3 (pl) 2006-11-10 2007-10-25 Usuwanie glikoalkoidów
PL07834645T PL2083636T3 (pl) 2006-11-10 2007-10-25 Usuwanie glikoalkaloidów
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CA2669090A CA2669090C (en) 2006-11-10 2007-10-25 Protein gel formation
US12/514,210 US9102749B2 (en) 2006-11-10 2007-10-25 Protein gel formation
US13/919,802 US20130281669A1 (en) 2006-11-10 2013-06-17 Native potato protein isolates
US14/722,906 US9968118B2 (en) 2006-11-10 2015-05-27 Protein gel formation

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US20100040591A1 (en) 2010-02-18
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CA2669096C (en) 2015-06-16
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EP1974615A1 (en) 2008-10-01
WO2008069650A1 (en) 2008-06-12
ATE451842T1 (de) 2010-01-15
US20100003394A1 (en) 2010-01-07
US9968118B2 (en) 2018-05-15
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US20150257416A1 (en) 2015-09-17
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US9102749B2 (en) 2015-08-11
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